ID S6CEQ1_9GAMM Unreviewed; 457 AA.
AC S6CEQ1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=M16 family peptidase {ECO:0000313|EMBL:BAN68255.1};
DE EC=3.4.24.64 {ECO:0000313|EMBL:BAN68255.1};
GN ORFNames=EBS_0272 {ECO:0000313|EMBL:BAN68255.1};
OS endosymbiont of unidentified scaly snail isolate Monju.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN68255.1, ECO:0000313|Proteomes:UP000015562};
RN [1] {ECO:0000313|EMBL:BAN68255.1, ECO:0000313|Proteomes:UP000015562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Monju {ECO:0000313|EMBL:BAN68255.1};
RX PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., Watanabe T.,
RA Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., Nemoto S.,
RA Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT "Allying with armored snails: the complete genome of gammaproteobacterial
RT endosymbiont.";
RL ISME J. 8:40-51(2014).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; AP012978; BAN68255.1; -; Genomic_DNA.
DR RefSeq; WP_043106971.1; NZ_AP012978.1.
DR AlphaFoldDB; S6CEQ1; -.
DR STRING; 1248727.EBS_0272; -.
DR MEROPS; M16.019; -.
DR KEGG; enm:EBS_0272; -.
DR HOGENOM; CLU_009902_1_0_6; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000015562; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAN68255.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000015562};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..457
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004547255"
FT DOMAIN 35..180
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 190..370
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 457 AA; 51056 MW; 1C1BEF3B591CD5F2 CRC64;
MFSRLLSVLL ALLPAIAAAG AAPVHEFLLD NGLKVIVKEE HRAPVAVSQV WYRIGSSYEE
GGRTGLSHLL EHMMFKGTRA HGPGEFSRIV AELGGSENAF TSRDYTAYFE TLSVEHLDRA
LELEADRMRN VVFEEKEFRK ELAVVMEERR MRTDDSPSGL TYEQLMAVAW RASPYQNPVI
GWMDDLANME IDALQRWYDF WYQPNNATLV VVGDVDPQQV LALAKKHFGP IPAGKVPAPR
RPAEPEQRGI TRVTVKAPAK QPYVLMGYKV PNLASAEHDW EPYALTVAAA VLDGGASARL
ARDLVRGRKI AASAGAQYDL YSRLPGLFLF DGTPTEGHRA AEVEQALREE VKRLQETLVS
REELDRVVTQ AVAAKVFQAD SIFYQAMEIG ILETIGLDWH LLEREIERLR AVTPEQVQAV
ARKYLKDDYL TVATLVPQPT DKPVRTTPIT RGTTHGK
//